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Volumn 134, Issue 2, 1996, Pages 401-411

Smoothelin, a novel cytoskeletal protein specific for smooth muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ; COMPLEMENTARY DNA; CYTOSKELETON PROTEIN; DYSTROPHIN; MESSENGER RNA; MONOCLONAL ANTIBODY; SPECTRIN; UTROPHIN;

EID: 0029952550     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.2.401     Document Type: Article
Times cited : (219)

References (52)
  • 2
    • 0019023345 scopus 로고
    • Purification of mouse immunoglobulin heavy chain messenger RNAs from total myeloma tumor RNA
    • Auffray, C., and F. Rougeon. 1980. Purification of mouse immunoglobulin heavy chain messenger RNAs from total myeloma tumor RNA. Eur. J. Biochem. 107:393-314.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 393-1314
    • Auffray, C.1    Rougeon, F.2
  • 4
    • 0015356037 scopus 로고
    • Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid cellulose
    • Aviv, A., and P. Leder. 1972. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid cellulose. Proc. Natl. Acad. Sci. USA. 69:1408-1412.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1408-1412
    • Aviv, A.1    Leder, P.2
  • 5
    • 0025130408 scopus 로고
    • Coexpression of α-sarcomeric, α-smooth muscle actin and desmin during myogenesis in rat and mouse embryos
    • Babai, F., J. Musevi-Aghdam, W. Schurch, A. Royal, and G. Gabbiani. 1990. Coexpression of α-sarcomeric, α-smooth muscle actin and desmin during myogenesis in rat and mouse embryos. Differentiation. 44:132-142.
    • (1990) Differentiation , vol.44 , pp. 132-142
    • Babai, F.1    Musevi-Aghdam, J.2    Schurch, W.3    Royal, A.4    Gabbiani, G.5
  • 6
    • 0023632004 scopus 로고
    • The sequence of α-actinin reveals homologies to spectrin and calmodulin
    • Baron, M.D., M.D. Davison, P. Jones, and P.R. Critchley. 1987. The sequence of α-actinin reveals homologies to spectrin and calmodulin. J. Biol. Chem. 262:17623-17629.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17623-17629
    • Baron, M.D.1    Davison, M.D.2    Jones, P.3    Critchley, P.R.4
  • 7
    • 0026786782 scopus 로고
    • Cloning and characterization of two human skeletal muscle α-actinin genes located on chromosomes 1 and 11
    • Beggs, A.H., T.J. Byers, J.H.M. Knoll, F.M. Boyce, G.A.P. Bruns, and L.M. Kunkel. 1992. Cloning and characterization of two human skeletal muscle α-actinin genes located on chromosomes 1 and 11. J. Biol. Chem. 267:9281-9288.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9281-9288
    • Beggs, A.H.1    Byers, T.J.2    Knoll, J.H.M.3    Boyce, F.M.4    Bruns, G.A.P.5    Kunkel, L.M.6
  • 10
    • 0019826503 scopus 로고
    • Smooth muscle phenotypic modulation: Role in atherogenesis
    • Campbell, G.R., and J.H. Chamley-Campbell. 1981. Smooth muscle phenotypic modulation: role in atherogenesis. Med. Hypothesis. 7:729-735.
    • (1981) Med. Hypothesis , vol.7 , pp. 729-735
    • Campbell, G.R.1    Chamley-Campbell, J.H.2
  • 11
    • 0024418964 scopus 로고
    • Cytodifferentiation and expression of α-smooth muscle actin mRNA and protein during primary culture of aortic smooth muscle cells: Correlation with cell density and proliferative state
    • Campbell, J.H., O. Kocher, O. Skalli, G. Gabbiani, and G.R. Campbell. 1989. Cytodifferentiation and expression of α-smooth muscle actin mRNA and protein during primary culture of aortic smooth muscle cells: correlation with cell density and proliferative state. Atherosclerosis. 9:633-643.
    • (1989) Atherosclerosis , vol.9 , pp. 633-643
    • Campbell, J.H.1    Kocher, O.2    Skalli, O.3    Gabbiani, G.4    Campbell, G.R.5
  • 12
    • 0008596570 scopus 로고
    • Experimental analysis of cytoskeletal function in early Xenopus laevis embryos
    • Chu, D.T.W., and M.W. Klymkowsky. 1987. Experimental analysis of cytoskeletal function in early Xenopus laevis embryos. Development. 8:140-142.
    • (1987) Development , vol.8 , pp. 140-142
    • Chu, D.T.W.1    Klymkowsky, M.W.2
  • 14
    • 0025848106 scopus 로고
    • The spectrin super-family
    • Dhermy, D. 1991. The spectrin super-family. Biol. Cell. 71:249-254.
    • (1991) Biol. Cell. , vol.71 , pp. 249-254
    • Dhermy, D.1
  • 15
    • 0027787707 scopus 로고
    • Calponin and SM22 as differentiation markers of smooth muscle markers: Spatiotemporal distribution during avian embryonic development
    • Duband, J.-L., M. Gimona, S. Scatena, and J.V. Small. 1993. Calponin and SM22 as differentiation markers of smooth muscle markers: spatiotemporal distribution during avian embryonic development. Differentiation. 55:1-11.
    • (1993) Differentiation , vol.55 , pp. 1-11
    • Duband, J.-L.1    Gimona, M.2    Scatena, S.3    Small, J.V.4
  • 16
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A.P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6-12.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-12
    • Feinberg, A.P.1    Vogelstein, B.2
  • 17
    • 0026757718 scopus 로고
    • Phenotypic changes of human smooth muscle cells during development: Late expression of heavy caldesmon and calponin
    • Frid, M.G., B.V. Shekhonin, V.E. Koteliansky, and M.A, Glukhova. 1992. Phenotypic changes of human smooth muscle cells during development: late expression of heavy caldesmon and calponin. Dev. Biol. 153:185-193.
    • (1992) Dev. Biol. , vol.153 , pp. 185-193
    • Frid, M.G.1    Shekhonin, B.V.2    Koteliansky, V.E.3    Glukhova, M.A.4
  • 20
    • 0019351935 scopus 로고
    • SV40-transformed simian cells support the replication of early SV40 mutants
    • Gluzman, Y. 1981. SV40-transformed simian cells support the replication of early SV40 mutants. Cell. 23:175-182.
    • (1981) Cell , vol.23 , pp. 175-182
    • Gluzman, Y.1
  • 21
    • 0025303805 scopus 로고
    • Differential control of tropomyosin mRNA levels during myogenesis suggests the existence of an isoform competition-autoregulation compensation control mechanism
    • Gunning, P., M. Gordon, R. Wade, R. Gahlmann, C.-S. Lin, and E. Hardeman. 1990. Differential control of tropomyosin mRNA levels during myogenesis suggests the existence of an isoform competition-autoregulation compensation control mechanism. Dev. Biol. 138:443-453.
    • (1990) Dev. Biol. , vol.138 , pp. 443-453
    • Gunning, P.1    Gordon, M.2    Wade, R.3    Gahlmann, R.4    Lin, C.-S.5    Hardeman, E.6
  • 23
    • 0025290039 scopus 로고
    • The identification and sequence of the actin-binding domain of human red blood cell β-spectrin
    • Karinch, A.M., W.E. Zimmer, and S.R. Goodman. 1990. The identification and sequence of the actin-binding domain of human red blood cell β-spectrin. J. Biol. Chem. 265:11833-11840.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11833-11840
    • Karinch, A.M.1    Zimmer, W.E.2    Goodman, S.R.3
  • 24
    • 0017232346 scopus 로고
    • Properties of a clonal muscle cell line from rat heart
    • Kimes, B.W., and B.L. Brandt. 1976. Properties of a clonal muscle cell line from rat heart. Exp. Cell Res. 98:367-381.
    • (1976) Exp. Cell Res. , vol.98 , pp. 367-381
    • Kimes, B.W.1    Brandt, B.L.2
  • 25
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod shaped cytoskeletal protein
    • Koening, M., A.P. Monaco, and L.M. Kunkel. 1988. The complete sequence of dystrophin predicts a rod shaped cytoskeletal protein. Cell. 53:219-228.
    • (1988) Cell , vol.53 , pp. 219-228
    • Koening, M.1    Monaco, A.P.2    Kunkel, L.M.3
  • 26
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köhler, G., and C. Milstein. 1975. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature (Lond). 256:495-497.
    • (1975) Nature (Lond) , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the heads of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the heads of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0023655235 scopus 로고
    • An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscle
    • Lees-Miller, J.P., D.H. Heeley, and L.B. Smillie. 1987. An abundant and novel protein of 22 kDa (SM22) is widely distributed in smooth muscle. Biochem. J. 244:705-709.
    • (1987) Biochem. J. , vol.244 , pp. 705-709
    • Lees-Miller, J.P.1    Heeley, D.H.2    Smillie, L.B.3
  • 29
    • 0026355337 scopus 로고
    • A comprehensive analysis of the developmental and tissue-specific expression of the isoactin multigene family in the rat
    • McHugh, K.M., K. Crawford, and J.L. Lessard. 1991. A comprehensive analysis of the developmental and tissue-specific expression of the isoactin multigene family in the rat. Dev. Biol. 148:442-458.
    • (1991) Dev. Biol. , vol.148 , pp. 442-458
    • McHugh, K.M.1    Crawford, K.2    Lessard, J.L.3
  • 30
    • 0024370066 scopus 로고
    • Identification of two types of smooth muscle myosin heavy chain isoforms by cDNA cloning and immunoblot analysis
    • Nagai, R., M. Kuro-O, P. Babij, and M. Periassamy. 1989. Identification of two types of smooth muscle myosin heavy chain isoforms by cDNA cloning and immunoblot analysis. J. Biol. Chem. 264:9734-9737.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9734-9737
    • Nagai, R.1    Kuro-O, M.2    Babij, P.3    Periassamy, M.4
  • 31
    • 0025995499 scopus 로고
    • Immunofluorescent study of heterogeneity in smooth muscle cells of human fetal vessels using antibodies to myosin, desmin, and vimentin
    • Nanaev, A.K., V.P. Shirinsky, and K.G. Birukov. 1991. Immunofluorescent study of heterogeneity in smooth muscle cells of human fetal vessels using antibodies to myosin, desmin, and vimentin. Cell Tissue Res. 266:535-540.
    • (1991) Cell Tissue Res. , vol.266 , pp. 535-540
    • Nanaev, A.K.1    Shirinsky, V.P.2    Birukov, K.G.3
  • 32
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of protein
    • O'Farrell, P.H. 1975. High resolution two-dimensional electrophoresis of protein. J. Biol. Chem. 230:4007-4021.
    • (1975) J. Biol. Chem. , vol.230 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 33
    • 0029048550 scopus 로고
    • Regulation of differentiation of vascular smooth muscle cells
    • Owens, G.K. 1995. Regulation of differentiation of vascular smooth muscle cells. Physiol. Rev. 75:487-517.
    • (1995) Physiol. Rev. , vol.75 , pp. 487-517
    • Owens, G.K.1
  • 34
    • 0017594823 scopus 로고
    • Enzymatic conversion of proteins to glycoproteins
    • Pless, D.D., and W.J. Lennarz. 1977. Enzymatic conversion of proteins to glycoproteins. Proc. Natl. Acad. Sci. USA. 74:134-138.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 134-138
    • Pless, D.D.1    Lennarz, W.J.2
  • 35
    • 0020769815 scopus 로고
    • Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence
    • Quax-Jeuken, Y.E.F.M., W.J. Quax, and H. Bloemendal. 1983. Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence. Proc. Natl. Acad. Sci. USA. 80:3548-3552.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3548-3552
    • Quax-Jeuken, Y.E.F.M.1    Quax, W.J.2    Bloemendal, H.3
  • 36
    • 0020960739 scopus 로고
    • Antibodies to intermediate filament proteins in the immunohistochemical identification of human tumours: An overview
    • Ramaekers, F.C.S., J.J.G. Puts, O. Moesker, A. Kant, P.H,K. Jap, C. Herman, and G.P. Vooijs. 1983. Antibodies to intermediate filament proteins in the immunohistochemical identification of human tumours: an overview. Histochem. J. 15:691-713.
    • (1983) Histochem. J. , vol.15 , pp. 691-713
    • Ramaekers, F.C.S.1    Puts, J.J.G.2    Moesker, O.3    Kant, A.4    Jap, P.H.K.5    Herman, C.6    Vooijs, G.P.7
  • 38
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., and C. Sander. 1993. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 39
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost, B., and C. Sander. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 19:55-77.
    • (1994) Proteins , vol.19 , pp. 55-77
    • Rost, B.1    Sander, C.2
  • 41
    • 0019162146 scopus 로고
    • Cloning a single stranded bacteriophage as an aid to rapid DNA sequencing
    • Sanger, F., A.R. Coulson, B.G. Barrell, A.J.H. Smith, and B.A. Roe. 1980. Cloning a single stranded bacteriophage as an aid to rapid DNA sequencing. J. Mol. Biol. 143:161-178.
    • (1980) J. Mol. Biol. , vol.143 , pp. 161-178
    • Sanger, F.1    Coulson, A.R.2    Barrell, B.G.3    Smith, A.J.H.4    Roe, B.A.5
  • 43
    • 0022881517 scopus 로고
    • A monoclonal antibody against α-smooth muscle actin: A new probe for smooth muscle differentiation
    • Skalli, O., P. Ropraz, A. Trzeciak, G. Benzonana, G. Gillesen, and G. Gabbiani. 1986. A monoclonal antibody against α-smooth muscle actin: a new probe for smooth muscle differentiation. J. Cell Biol. 103:2787-2796.
    • (1986) J. Cell Biol. , vol.103 , pp. 2787-2796
    • Skalli, O.1    Ropraz, P.2    Trzeciak, A.3    Benzonana, G.4    Gillesen, G.5    Gabbiani, G.6
  • 44
    • 0023712543 scopus 로고
    • Vascular smooth muscle calponin: A novel T-like protein
    • Takahashi, K., K. Hiwada, and T. Kokuhu. 1988. Vascular smooth muscle calponin: a novel T-like protein. Hypertension. 11:620-626.
    • (1988) Hypertension , vol.11 , pp. 620-626
    • Takahashi, K.1    Hiwada, K.2    Kokuhu, T.3
  • 45
    • 0025959229 scopus 로고
    • Co-localization of immunoreactive forms of calponin with actin cytoskeleton in platelets, fibroblasts and smooth muscle
    • Takeuchi, K., K. Takahashi, M. Abe, W. Nishida, K. Hiwada, T. Nabeya, and K. Maruyama. 1991. Co-localization of immunoreactive forms of calponin with actin cytoskeleton in platelets, fibroblasts and smooth muscle. J. Biochem. 109:311-316.
    • (1991) J. Biochem. , vol.109 , pp. 311-316
    • Takeuchi, K.1    Takahashi, K.2    Abe, M.3    Nishida, W.4    Hiwada, K.5    Nabeya, T.6    Maruyama, K.7
  • 47
    • 0024344131 scopus 로고
    • Detection of metavinculin in human platelets using a modified talin overlay assay
    • Turner, C.E., and K. Burridge. 1989. Detection of metavinculin in human platelets using a modified talin overlay assay. Eur. J. Cell Biol. 49:202-206.
    • (1989) Eur. J. Cell Biol. , vol.49 , pp. 202-206
    • Turner, C.E.1    Burridge, K.2
  • 48
    • 0027407773 scopus 로고
    • Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs
    • Vaughan, K.T., F.E. Weber, S. Einheber, and D.A. Fischman. 1993. Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. J. Biol. Chem. 268:3670-3676.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3670-3676
    • Vaughan, K.T.1    Weber, F.E.2    Einheber, S.3    Fischman, D.A.4


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